› 3re3

X-ray diffraction
2.64Å resolution

Crystal Structure of 2-C-Methyl-D-Erythritol 2,4-Cyclodiphosphate Synthase from Francisella tularensis

Released:
DOI: 10.2210/pdb3re3/pdb
PDB entry 3re3 coloured by chain, front view.
PDB entry 3re3 coloured by chain, side view.
PDB entry 3re3 coloured by chain, top view.
Source organism: Francisella tularensis subsp. tularensis SCHU S4
Entry authors: Kim Y, Makowska-Grzyska M, Kwon K, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed: 
2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo dodecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-177673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 162 amino acids
Theoretical weight: 18.15 KDa
Source organism: Francisella tularensis subsp. tularensis SCHU S4
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5NFU1 (Residues: 1-159; Coverage: 100%)
Gene names: FTT_1128, ispF
Sequence domains: YgbB family
Structure domains: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Ligands and Environments

5 bound ligands:
Ligand POP 2 x POP
Ligand NA 3 x NA
Ligand CL 2 x CL
Ligand PO4 3 x PO4
Ligand MPD 2 x MPD
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P63
Unit cell:
a: 96.116Å b: 96.116Å c: 155.308Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.173 0.227
Expression system: Escherichia coli

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